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SALTY:PEPE

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Species (Taxon ID) Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). (99287)
Gene Name(s) pepE
Protein Name(s) Peptidase E

Alpha-aspartyl dipeptidase Asp-specific dipeptidase Dipeptidase E

External Links
UniProt P36936
EMBL U01246
AE006468
PIR A36867
RefSeq NP_463055.1
PDB 1FY2
1FYE
PDBsum 1FY2
1FYE
ProteinModelPortal P36936
SMR P36936
STRING 99287.STM4190
MEROPS S51.001
PRIDE P36936
EnsemblBacteria AAL23014
GeneID 1255716
KEGG stm:STM4190
PATRIC 32387273
HOGENOM HOG000281834
KO K05995
OMA TPYIGWS
OrthoDB EOG6M6JST
PhylomeDB P36936
BioCyc SENT99287:GCTI-4220-MONOMER
EvolutionaryTrace P36936
Proteomes UP000001014
GO GO:0005737
GO:0016805
GO:0008236
Gene3D 3.40.50.880
HAMAP MF_00510
InterPro IPR029062
IPR005320
IPR023172
Pfam PF03575
SUPFAM SSF52317

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016805

dipeptidase activity

PMID:10762256[1]

ECO:0000314

F

Table 4 shows that Peptidase E cleaved several types of dipeptides. It did cleave one type of tripeptide, but this is most likely because it is smallest aspartyl tripeptide.

complete

GO:0016787

hydrolase activity

PMID:10762256[1]

ECO:0000315

F

Figure 3 shows that none of the mutant phenotypes of peptidase E hydrolyze Asp-pNA as well as the wild type.

complete

enables

GO:0008233

peptidase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11920
PANTHER:PTN001073551

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005320

P

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005320

F

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023172

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103203

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103203

P

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103203

F

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0224

F

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0720

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Lassy, RA & Miller, CG (2000) Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase. J. Bacteriol. 182 2536-43 PubMed GONUTS page
  2. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page